Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF)

Radixin is a member of the ERM proteins, which cross‐link plasma membranes and actin filaments. The N‐terminal FERM domains of ERM proteins interact with Na+/H+‐exchanger regulatory factors (NHERFs), which are PDZ‐containing adaptor proteins, to modulate the ion‐channel activity. Here, crystals of c...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-01, Vol.59 (1), p.177-179
Hauptverfasser: Terawaki, Shin-ichi, Maesaki, Ryoko, Okada, Kengo, Hakoshima, Toshio
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Sprache:eng
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Zusammenfassung:Radixin is a member of the ERM proteins, which cross‐link plasma membranes and actin filaments. The N‐terminal FERM domains of ERM proteins interact with Na+/H+‐exchanger regulatory factors (NHERFs), which are PDZ‐containing adaptor proteins, to modulate the ion‐channel activity. Here, crystals of complexes between the radixin FERM domain and the C‐terminal regions of NHERF and NHERF2 have been obtained. The crystals of the FERM–NHERF complex were found to belong to space group P212121, with unit‐cell parameters a = 69.38 (2), b = 146.27 (4), c = 177.76 (7) Å. The crystal contains four complexes in the asymmetric unit. An intensity data set was collected to a resolution of 2.50 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902019686